Please use this identifier to cite or link to this item:
|標題:||Direct interaction of focal adhesion kinase (FAK) with Met is required for FAK to promote hepatocyte growth factor-induced cell invasion||作者:||Chen, S.Y.
|關鍵字:||receptor tyrosine kinase;c-met;ferm domain;oncogenic rearrangement;terminal domain;protein;gab1;phosphorylation;activation;motility||Project:||Molecular and Cellular Biology||期刊/報告no：:||Molecular and Cellular Biology, Volume 26, Issue 13, Page(s) 5155-5167.||摘要:||
Focal adhesion kinase (FAK) has been implicated to be a point of convergence of integrin and growth factor signaling pathways. Here we report that FAK directly interacts with the hepatocyte growth factor receptor c-Met. Phosphorylation of c-Met at Tyr-1349 and, to a lesser extent, Tyr-1356 is required for its interaction with the band 4.1 and ezrin/radixin/moesin homology domain (FERM domain) of FAK. The F2 subdomain of the FAK FERM domain alone is sufficient for Met binding, in which a patch of basic residues ((216)KAKTLRK(222)) are critical for the interaction. Met-FAK interaction leads to FAK activation and subsequent contribution to hepatocyte growth factor-induced cell motility and cell invasion. Our results provide evidence that constitutive Met-FAK interaction may be a critical determinant for tumor cells to acquire invasive potential.
|Appears in Collections:||生命科學院|
Show full item record
TAIR Related Article
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.